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Journal of Virology, January 2005, p. 800-811, Vol. 79, No. 2
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.2.800-811.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Virion Proteins of Kaposi's Sarcoma-Associated Herpesvirus

Fan Xiu Zhu,1 Jae Min Chong,1 Lijun Wu,2 and Yan Yuan1*

Department of Microbiology, University of Pennsylvania School of Dental Medicine, Philadelphia, Pennsylvania,1 Promab Biotechnologies, Inc., Hayward, California2

Received 19 July 2004/ Accepted 8 October 2004

The proteins that compose a herpesvirus virion are thought to contain the functional information required for de novo infection, as well as virion assembly and egress. To investigate functional roles of Kaposi's sarcoma-associated herpesvirus (KSHV) virion proteins in viral productive replication and de novo infection, we attempted to identify virion proteins from purified KSHV by a proteomic approach. Extracellular KSHV virions were purified from phorbol-12-tetradecanoate-13-acetate-induced BCBL-1 cells through double-gradient ultracentrifugation, and their component proteins were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Thirty prominent protein bands were excised and subjected to high-performance liquid chromatography ion trap mass spectrometric analysis. This study led to the identification of 24 virion-associated proteins. These include five capsid proteins, eight envelope glycoproteins, six tegument proteins, and five proteins whose locations in the virions have not yet been defined. Putative tegument proteins encoded by open reading frame 21 (ORF21), ORF33, and ORF45 were characterized and found to be resistant to protease digestion when purified virions were treated with trypsin, confirming that they are located within the virion particles. The ORF64-encoded large tegument protein was found to be associated with capsid but sensitive to protease treatment, suggesting its unique structure and array in KSHV virions. In addition, cellular ß-actin and class II myosin heavy chain type A were found inside KSHV virions and associated with tegument-capsid structure. Identification of KSHV virion proteins makes it possible to study the functional roles of these virion proteins in KSHV replication and pathogenicity.

* Corresponding author. Mailing address: Department of Microbiology, School of Dental Medicine, University of Pennsylvania, 240 S. 40th St., Philadelphia, PA 19104. Phone: (215) 573-7556. Fax: (215) 898-8385. E-mail: yuan2{at}pobox.upenn.edu.

Journal of Virology, January 2005, p. 800-811, Vol. 79, No. 2
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.2.800-811.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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